Data concerning secondary structure and alpha-glucans-binding capacity of the LaCBM26

Data concerning secondary structure and alpha-glucans-binding capacity of the LaCBM26

Carbohydrate-binding modules (CBMs) are auxiliary domains into glycoside-hydrolases that allow the interaction between the insoluble substrate and the solubilized enzyme, through hydrophobic, CH-π interactions and hydrogen bonds. Here, we present the data article related to the interaction of one La...

Full description

Bibliographic Details
Main Authors: Silvia Armenta, Zaira Sánchez-Cuapio, Amelia Farrés, Karen Manoutcharian, Alejandra Hernandez-Santoyo, Sergio Sánchez, Romina Rodríguez-Sanoja
Format: Article
Language:English
Published: Elsevier 2018-12-01
Series:Data in Brief
Online Access:http://www.sciencedirect.com/science/article/pii/S2352340918314495
id doaj-c43e3a91fe784dc1b3d7d3fdd43d6e14
record_format Article
spelling doaj-c43e3a91fe784dc1b3d7d3fdd43d6e142020-11-25T02:21:00ZengElsevierData in Brief2352-34092018-12-012119441949Data concerning secondary structure and alpha-glucans-binding capacity of the LaCBM26Silvia Armenta0Zaira Sánchez-Cuapio1Amelia Farrés2Karen Manoutcharian3Alejandra Hernandez-Santoyo4Sergio Sánchez5Romina Rodríguez-Sanoja6Instituto de Investigaciones Biomédicas, Universidad Nacional Autónoma de México (UNAM), A.P. 70228, Ciudad Universitaria, Ciudad de México 04510, México; Programa de Doctorado en Ciencias Bioquímicas, Universidad Nacional Autónoma de México (UNAM), A.P. 70228, Ciudad Universitaria, México DF 04510, MexicoInstituto de Investigaciones Biomédicas, Universidad Nacional Autónoma de México (UNAM), A.P. 70228, Ciudad Universitaria, Ciudad de México 04510, México; Programa de Doctorado en Ciencias Biomédicas, Universidad Nacional Autónoma de México (UNAM), A.P. 70228, Ciudad Universitaria, México DF 04510, MexicoFacultad de Química, Universidad Nacional Autónoma de México, Circuito Exterior s/n Ciudad Universitaria, Ciudad de México 04510, MéxicoInstituto de Investigaciones Biomédicas, Universidad Nacional Autónoma de México (UNAM), A.P. 70228, Ciudad Universitaria, Ciudad de México 04510, MéxicoInstituto de Química, Universidad Nacional Autónoma de México, Circuito Exterior s/n Ciudad Universitaria, Ciudad de México 04510, MéxicoInstituto de Investigaciones Biomédicas, Universidad Nacional Autónoma de México (UNAM), A.P. 70228, Ciudad Universitaria, Ciudad de México 04510, MéxicoInstituto de Investigaciones Biomédicas, Universidad Nacional Autónoma de México (UNAM), A.P. 70228, Ciudad Universitaria, Ciudad de México 04510, México; Corresponding author.Carbohydrate-binding modules (CBMs) are auxiliary domains into glycoside-hydrolases that allow the interaction between the insoluble substrate and the solubilized enzyme, through hydrophobic, CH-π interactions and hydrogen bonds. Here, we present the data article related to the interaction of one LaCBM26 and some mutated proteins with soluble α-glucans determined by enzyme-linked carbohydrate-binding assay, isothermal titration calorimetry (ITC), and affinity gel electrophoresis (AGE). The data of the behavior of proteins in presence and absence of substrate analyzed by circular dichroism CD and thermofluor are also presented. These results are complementary to the research article “The role of conserved non-aromatic residues in the Lactobacillus amylovorus α-amylase CBM26-starch interaction” (Armenta et al., 2019). Keywords: Carbohydrate-binding module, Starch, α-Glucans recognitionhttp://www.sciencedirect.com/science/article/pii/S2352340918314495
collection DOAJ
language English
format Article
sources DOAJ
author Silvia Armenta
Zaira Sánchez-Cuapio
Amelia Farrés
Karen Manoutcharian
Alejandra Hernandez-Santoyo
Sergio Sánchez
Romina Rodríguez-Sanoja
spellingShingle Silvia Armenta
Zaira Sánchez-Cuapio
Amelia Farrés
Karen Manoutcharian
Alejandra Hernandez-Santoyo
Sergio Sánchez
Romina Rodríguez-Sanoja
Data concerning secondary structure and alpha-glucans-binding capacity of the LaCBM26
Data in Brief
author_facet Silvia Armenta
Zaira Sánchez-Cuapio
Amelia Farrés
Karen Manoutcharian
Alejandra Hernandez-Santoyo
Sergio Sánchez
Romina Rodríguez-Sanoja
author_sort Silvia Armenta
title Data concerning secondary structure and alpha-glucans-binding capacity of the LaCBM26
title_short Data concerning secondary structure and alpha-glucans-binding capacity of the LaCBM26
title_full Data concerning secondary structure and alpha-glucans-binding capacity of the LaCBM26
title_fullStr Data concerning secondary structure and alpha-glucans-binding capacity of the LaCBM26
title_full_unstemmed Data concerning secondary structure and alpha-glucans-binding capacity of the LaCBM26
title_sort data concerning secondary structure and alpha-glucans-binding capacity of the lacbm26
publisher Elsevier
series Data in Brief
issn 2352-3409
publishDate 2018-12-01
description Carbohydrate-binding modules (CBMs) are auxiliary domains into glycoside-hydrolases that allow the interaction between the insoluble substrate and the solubilized enzyme, through hydrophobic, CH-π interactions and hydrogen bonds. Here, we present the data article related to the interaction of one LaCBM26 and some mutated proteins with soluble α-glucans determined by enzyme-linked carbohydrate-binding assay, isothermal titration calorimetry (ITC), and affinity gel electrophoresis (AGE). The data of the behavior of proteins in presence and absence of substrate analyzed by circular dichroism CD and thermofluor are also presented. These results are complementary to the research article “The role of conserved non-aromatic residues in the Lactobacillus amylovorus α-amylase CBM26-starch interaction” (Armenta et al., 2019). Keywords: Carbohydrate-binding module, Starch, α-Glucans recognition
url http://www.sciencedirect.com/science/article/pii/S2352340918314495
work_keys_str_mv AT silviaarmenta dataconcerningsecondarystructureandalphaglucansbindingcapacityofthelacbm26
AT zairasanchezcuapio dataconcerningsecondarystructureandalphaglucansbindingcapacityofthelacbm26
AT ameliafarres dataconcerningsecondarystructureandalphaglucansbindingcapacityofthelacbm26
AT karenmanoutcharian dataconcerningsecondarystructureandalphaglucansbindingcapacityofthelacbm26
AT alejandrahernandezsantoyo dataconcerningsecondarystructureandalphaglucansbindingcapacityofthelacbm26
AT sergiosanchez dataconcerningsecondarystructureandalphaglucansbindingcapacityofthelacbm26
AT rominarodriguezsanoja dataconcerningsecondarystructureandalphaglucansbindingcapacityofthelacbm26
_version_ 1724868233720233984

Similar Items